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  Capturing Functionally Relevant Protein Motions at the Atomic Level: Femtosecond Time Resolved Serial Crystallography of Ligand Dissociation of Carboxy-Myoglobin

Müller-Werkmeister, H. M., Kuo, A., Ginn, H. M., Oghbaey, S., Sarracini, A., Pare-Labrosse, O., et al. (2016). Capturing Functionally Relevant Protein Motions at the Atomic Level: Femtosecond Time Resolved Serial Crystallography of Ligand Dissociation of Carboxy-Myoglobin. Biophysical Journal, 110(3), 513a. doi:10.1016/j.bpj.2015.11.2745.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-44F7-B Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-44F8-9
Genre: Conference Paper

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 Creators:
Müller-Werkmeister, Henrike M.1, 2, Author
Kuo, Anling2, Author
Ginn, Helen M.3, Author
Oghbaey, Saeed1, Author
Sarracini, Antoine1, Author
Pare-Labrosse, Olivier1, Author
Sherrell, Darren4, Author
Marx, Alexander5, Author              
Epp, Sascha W.5, Author              
Pearson, Arwen R.6, Author
Owen, Robin L. 4, Author
Stuart, David I.3, Author
Ernst, Oliver P.2, Author
Miller, R. J. Dwayne5, Author              
Affiliations:
1Chemistry & Physics, University of Toronto, Toronto, ON, Canada, ou_persistent22              
2Biochemistry, University of Toronto, Toronto, ON, Canada, ou_persistent22              
3University of Oxford, Oxford, United Kingdom, ou_persistent22              
4Diamond Light Source, Didcot, United Kingdom, ou_persistent22              
5Miller Group, Atomically Resolved Dynamics Department, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society, ou_1938288              
6Hamburg Centre for Ultrafast Imaging, University of Hamburg, Hamburg, Germany, ou_persistent22              

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Free keywords: Femtosecond;Crystallography;Carboxy-Myoglobin
 Abstract: The recent advent of X-Ray free electron lasers with highest brilliance and femtosecond pulses opens new possibilities for time-resolved protein crystallography [Miller, R.J.D, Science, 2014, 343, 1108-1116]. A fundamental biophysical question becomes accessible experimentally now: The investigation of protein dynamics with all atomic resolution on the shortest biochemically relevant timescale around 100 fs. Here is where bond-breaking events occur, which in turn translate into secondary and tertiary structure changes and cause a protein to fulfill its function over a wide range of timescales.

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Language(s): eng - English
 Dates: 2016-02-16
 Publication Status: Published online
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: No review
 Identifiers: DOI: 10.1016/j.bpj.2015.11.2745
 Degree: -

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Title: Biophysical Journal
  Abbreviation : Biophys. J.
Source Genre: Journal
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Publ. Info: Cambridge, Mass. : Cell Press
Pages: - Volume / Issue: 110 (3) Sequence Number: - Start / End Page: 513a Identifier: Other: 0006-3495
CoNE: /journals/resource/954925385117